Recent advances in understanding catalysis of protein folding by molecular chaperones
Molecular chaperones are highly conserved proteins that promote proper folding of other
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …
Advances in hydrogen/deuterium exchange mass spectrometry and the pursuit of challenging biological systems
EI James, TA Murphree, C Vorauer, JR Engen… - Chemical …, 2021 - ACS Publications
Solution-phase hydrogen/deuterium exchange (HDX) coupled to mass spectrometry (MS) is
a widespread tool for structural analysis across academia and the biopharmaceutical …
a widespread tool for structural analysis across academia and the biopharmaceutical …
Molecular dissection of amyloid disaggregation by human HSP70
AS Wentink, NB Nillegoda, J Feufel, G Ubartaitė… - Nature, 2020 - nature.com
The deposition of highly ordered fibrillar-type aggregates into inclusion bodies is a hallmark
of neurodegenerative diseases such as Parkinson's disease. The high stability of such …
of neurodegenerative diseases such as Parkinson's disease. The high stability of such …
[HTML][HTML] Chaperones directly and efficiently disperse stress-triggered biomolecular condensates
Stresses such as heat shock trigger the formation of protein aggregates and the induction of
a disaggregation system composed of molecular chaperones. Recent work reveals that …
a disaggregation system composed of molecular chaperones. Recent work reveals that …
Structure of the M. tuberculosis DnaK−GrpE complex reveals how key DnaK roles are controlled
X Xiao, A Fay, PS Molina, A Kovach… - Nature …, 2024 - nature.com
The molecular chaperone DnaK is essential for viability of Mycobacterium tuberculosis
(Mtb). DnaK hydrolyzes ATP to fold substrates, and the resulting ADP is exchanged for ATP …
(Mtb). DnaK hydrolyzes ATP to fold substrates, and the resulting ADP is exchanged for ATP …
The function, structure, and origins of the ER membrane protein complex
RS Hegde - Annual Review of Biochemistry, 2022 - annualreviews.org
The endoplasmic reticulum (ER) is the site of membrane protein insertion, folding, and
assembly in eukaryotes. Over the past few years, a combination of genetic and biochemical …
assembly in eukaryotes. Over the past few years, a combination of genetic and biochemical …
J-domain protein chaperone circuits in proteostasis and disease
The J-domain proteins (JDP) form the largest protein family among cellular chaperones. In
cooperation with the Hsp70 chaperone system, these co-chaperones orchestrate a plethora …
cooperation with the Hsp70 chaperone system, these co-chaperones orchestrate a plethora …
The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model
P Yuste-Checa, VA Trinkaus, I Riera-Tur… - Nature …, 2021 - nature.com
Spreading of aggregate pathology across brain regions acts as a driver of disease
progression in Tau-related neurodegeneration, including Alzheimer's disease (AD) and …
progression in Tau-related neurodegeneration, including Alzheimer's disease (AD) and …
The Hsp70-chaperone machines in bacteria
MP Mayer - Frontiers in Molecular Biosciences, 2021 - frontiersin.org
The ATP-dependent Hsp70s are evolutionary conserved molecular chaperones that
constitute central hubs of the cellular protein quality surveillance network. None of the other …
constitute central hubs of the cellular protein quality surveillance network. None of the other …
The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends
Molecular chaperones contribute to the maintenance of cellular protein homoeostasis
through assisting de novo protein folding and preventing amyloid formation. Chaperones of …
through assisting de novo protein folding and preventing amyloid formation. Chaperones of …